Information on EC 3.4.21.86 - Limulus clotting enzyme

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.86
-
RECOMMENDED NAME
GeneOntology No.
Limulus clotting enzyme
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of -Arg18-/- and -Arg47-/- bonds in coagulogen to form coagulin and fragments
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Leu-Gly-Arg-4-aminophenyl ester + H2O
benzyloxycarbonyl-Leu-Gly-Arg + 4-aminophenol
show the reaction diagram
-
-
-
-
?
Coagulogen + H2O
Coagulin + fragments
show the reaction diagram
-
-
-
-
Limulus amebocyte lysate + H2O
small particles of clotted enzyme
show the reaction diagram
-
bacterial endotoxins induce the formation of small particles of clotted enzyme
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bacterial endotoxins
-
-
-
additional information
-
activated by limulus clotting factor B
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
zymogen
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
inactive proenzyme, 1 * 54000, active enzyme, 1 * 25000 + 1 * 31000, SDS-PAGE
31000
-
inactive proenzyme, 1 * 54000, active enzyme, 1 * 25000 + 1 * 31000, SDS-PAGE
38190
-
Limulus sp., calculation from nucleotide sequence, mature protein
54000
-
SDS-PAGE, absence of 2-mercaptoethanol
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
inactive proenzyme, 1 * 54000, active enzyme, 1 * 25000 + 1 * 31000, SDS-PAGE
additional information
-
serine active site of enzyme is within the heavy chain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
inactive proenzyme of 54 kDa is converted to its active form of 25 kDa + 31 kDa by purified factor B or by trypsin. Heavy and light chain of active form are bridged by a disulfide linkage
additional information
-
does not contain gamma-carboxyglutamic acid
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of proclotting enzyme, the zymogen of clotting enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
screen-printed endotoxin sensor based on amperometric detection of protease activity. The amperometric measurement with a screen-printed electrode provides compact, low-cost, and easy-to-use sensors for on-site monitoring of endotoxin
molecular biology
-
laser scattering photometry can be used to measure the formation of small particles of clotted enzyme, the timing is related to endotoxin concentration, this method can be used for quick and sensitive endotoxin assay